Histone-lysine N-methyltransferase SETD2 (SETD2) is a 2564-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BYW2.
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The mean pLDDT of this model is 43.3 (very low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 12% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 78% |
What pLDDT means and how to read it
Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:16118227, PubMed:19141475, PubMed:21526191, PubMed:21792193, PubMed:23043551, PubMed:27474439). It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (PubMed:19332550). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (By similarity). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (PubMed:23325844). Acts as a key regulator of DNA mismatch repair in G1…
Specifically interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A): binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each heptad (PubMed:16118227, PubMed:16314571). Interacts with HTT (PubMed:10958656, PubMed:11461154, PubMed:9700202). Interacts with IWS1 (PubMed:19141475). Interacts with p53/TP53; leading to regulate…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5JLB | X-ray | 1.5 Å | A=1434-1711 |
| 5LT7 | X-ray | 1.51 Å | A=1433-1711 |
| 5LT8 | X-ray | 1.57 Å | A=1433-1711 |
| 7EVS | X-ray | 1.6 Å | C/D=2180-2192 |
| 5LSY | X-ray | 1.62 Å | A=1433-1711 |
| 5LSZ | X-ray | 1.62 Å | A=1433-1711 |
| 9G4A | X-ray | 1.65 Å | A=1433-1711 |
| 6J9J | X-ray | 1.78 Å | A=1447-1703 |
| 5LSS | X-ray | 1.79 Å | A=1433-1711 |
| 7EVR | X-ray | 1.8 Å | B/D=2167-2192 |
| 7LZD | X-ray | 1.8 Å | A=1434-1711 |
| 8Q5P | X-ray | 1.81 Å | A=1433-1711 |
| 9HGG | X-ray | 1.9 Å | B=1363-1379 |
| 4H12 | X-ray | 1.99 Å | A=1434-1711 |
| 5JJY | X-ray | 2.05 Å | A=1434-1711 |
| 5LT6 | X-ray | 2.05 Å | A/B=1433-1711 |
| 4FMU | X-ray | 2.1 Å | A=1434-1711 |
| 8RZU | X-ray | 2.19 Å | A=1433-1711 |
| 7LZB | X-ray | 2.28 Å | A=1434-1711 |
| 6VDB | X-ray | 2.3 Å | A=1433-1711 |
Showing 20 of 43 experimental structures (best resolution first).
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